大肠杆菌外膜脂蛋白上肽段延伸的氨基酸序列。
Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane.
作者信息
Inouye S, Wang S, Sekizawa J, Halegoua S, Inouye M
出版信息
Proc Natl Acad Sci U S A. 1977 Mar;74(3):1004-8. doi: 10.1073/pnas.74.3.1004.
Abstract
The messenger RNA for the lipoprotein of the E. coli outer membrane was found to code for a putative precursor, prolipoprotein, which has 20 additional amino acid residues extending from the amino terminus of the lipoprotein. Using the prolipoprotein synthesized in an E. coli cell-free system directed by purified messenger RNA for the lipoprotein, the complete amino acid sequence of the amino-terminal precursor region was determined to be as follows: (formula: see text). It was also found that the prolipoprotein that accumulates in toluene-treated cells has the same sequence. The significance of the amino acid sequence is discussed in terms of the mechanism of biosynthesis and assembly of the lipoprotein in the E. coli outer membrane.
摘要
人们发现，大肠杆菌外膜脂蛋白的信使核糖核酸编码一种假定的前体，即前脂蛋白，它从脂蛋白的氨基末端延伸出另外20个氨基酸残基。利用在无细胞体系中由纯化的脂蛋白信使核糖核酸指导合成的前脂蛋白，确定了氨基末端前体区域的完整氨基酸序列如下：（分子式：见正文）。还发现，在经甲苯处理的细胞中积累的前脂蛋白具有相同的序列。本文根据脂蛋白在大肠杆菌外膜中的生物合成和组装机制，讨论了该氨基酸序列的意义。
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